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- W2318662004 abstract "Chronic pain is the most ubiquitous disease with an incidence of 100 million people in the U.S. Opiate therapy is the mainly prescribed treatment for chronic neuropathic pain. However opioids do not address the mechanisms of neuropathic pain and thus have limited efficacy against this type of pain [1]. While opioids may reduce the pain states experienced by the patients, they have adverse effects such as tolerance, addiction, and medication overuse with long-term administration. It has been found that by blocking the κ opioid receptor (KOR) a reduction in tolerance and depressive affective states that can occur with opioid administration [2]. With this in mind we are working towards the development of a KOR selective antagonist with variable duration of action. Dynorphin A (Dyn A, Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-AsnGln) is one of three endogenous opioid peptides with high affinities for the μ (MOR), δ (DOR), and κ opioid receptors, with a preference for the KOR. Dyn A mediates an inhibitory effect through the opioid receptors resulting in nociception. Some have studied the importance of consecutive polar residues as is found in Dyn A and found that these were important for binding and function [3]. Dyn A has been extensively studied in the search for KOR ligands. Our approach is different in that our main target is a shorter peptide with an amino acid residue deletion in the middle of the sequence. The deleted residue happens to be one of the key residues determined by studies of the relative importance of the amino acid residues in Dyn A sequence. It was previously believed that residues Arg, Lys, and Lys were the most important residues for binding and potency at the KOR [4]. The importance of these residues was determined by the binding affinity of truncated analogs of Dyn A. In our approach we are completely deleting the amino acid residue and this is very interesting because usually residue deletions would have unfavorable effects to the binding of a peptide due to changes in conformation and charge distributions." @default.
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- W2318662004 date "2015-01-01" @default.
- W2318662004 modified "2023-09-26" @default.
- W2318662004 title "Structure-Activity Relationship Studies of Dynorphin A Analogs at the Kappa Opioid Receptor" @default.
- W2318662004 doi "https://doi.org/10.17952/24aps.2015.096" @default.
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